ID Q4VUJ0_RHIRO Unreviewed; 217 AA.
AC Q4VUJ0;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Growth hormone-like protein 2 {ECO:0000313|EMBL:AAU95550.1};
DE SubName: Full=Somatotropin-like {ECO:0000313|Ensembl:ENSRROP00000007626.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|EMBL:AAU95550.1};
RN [1] {ECO:0000313|EMBL:AAU95550.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15848116; DOI=10.1016/j.gene.2005.03.003;
RA Ye C., Li Y., Shi P., Zhang Y.P.;
RT "Molecular evolution of growth hormone gene family in old world monkeys and
RT hominoids.";
RL Gene 350:183-192(2005).
RN [2] {ECO:0000313|Ensembl:ENSRROP00000007626.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Plays an important role in growth control. Its major role in
CC stimulating body growth is to stimulate the liver and other tissues to
CC secrete IGF-1. It stimulates both the differentiation and proliferation
CC of myoblasts. It also stimulates amino acid uptake and protein
CC synthesis in muscle and other tissues. {ECO:0000256|ARBA:ARBA00025313}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU003618}.
CC -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC {ECO:0000256|ARBA:ARBA00008474, ECO:0000256|RuleBase:RU003618}.
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DR EMBL; AY621648; AAU95550.1; -; Genomic_DNA.
DR STRING; 61622.ENSRROP00000007626; -.
DR Ensembl; ENSRROT00000031260.1; ENSRROP00000007626.1; ENSRROG00000027808.1.
DR GeneTree; ENSGT00950000182818; -.
DR OMA; NSQVAFC; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005131; F:growth hormone receptor binding; IEA:InterPro.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd10285; somatotropin_like; 1.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR034975; Somatotropin.
DR InterPro; IPR001400; Somatotropin/Prolactin.
DR InterPro; IPR018116; Somatotropin_CS.
DR PANTHER; PTHR11417:SF2; SOMATOTROPIN; 1.
DR PANTHER; PTHR11417; SOMATOTROPIN,PROLACTIN; 1.
DR Pfam; PF00103; Hormone_1; 1.
DR PRINTS; PR00836; SOMATOTROPIN.
DR SUPFAM; SSF47266; 4-helical cytokines; 1.
DR PROSITE; PS00266; SOMATOTROPIN_1; 1.
DR PROSITE; PS00338; SOMATOTROPIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hormone {ECO:0000256|ARBA:ARBA00022702, ECO:0000256|RuleBase:RU003618};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601400-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PIRSR:PIRSR601400-1}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..217
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014586576"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR601400-1"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR601400-1"
SQ SEQUENCE 217 AA; 24854 MW; 6B34046F77735612 CRC64;
MAAGSRTSLL LAFALLCLPW LQEAGRVPSV PLSRLFDHAM IQAHRLHQLA FDTYQEFEET
YIPKEKKHSI MENPQASFCF SESIPTPANR EETQQKSNLE LLRISLLLIQ SWLEPVHLLG
SVFANNLVYG TSESDVYDLL KNLEEGIQTL MRRLEDGSPR TGQIFKQTYS KFDTDSHNDD
SLLKNYGLLH CFRKDMDMVE TFLRMVQCRS VEGSCGF
//
